Probing the reaction mechanism of IspH protein by x-ray structure analysis - Test2 - elhamkhani - TriplyDB

Probing the reaction mechanism of IspH protein by x-ray structure analysis

Probing the reaction mechanism of IspH protein by x-ray structure analysis

http://www.wikidata.org/entity/Q27658984

about

Discovery of acetylene hydratase activity of the iron–sulphur protein IspH Structures of Fluoro, Amino, and Thiol Inhibitors Bound to the [Fe4S4] Protein IspH Active-site models for complexes of quinolinate synthase with substrates and intermediates Are Free Radicals Involved in IspH Catalysis? An EPR and Crystallographic Investigation Insights into the Binding of Pyridines to the Iron–Sulfur Enzyme IspH Structure of the (E)-4-hydroxy-3-methyl-but-2-enyl-diphosphate reductase from Plasmodium falciparum New Insight into Isoprenoids Biosynthesis Process and Future Prospects for Drug Designing in Plasmodium Reconstruction and evaluation of the synthetic bacterial MEP pathway in Saccharomyces cerevisiae Utilizing a dynamical description of IspH to aid in the development of novel antimicrobial drugs Isoprenoid precursor biosynthesis offers potential targets for drug discovery against diseases caused by apicomplexan parasites Organometallic mechanism of action and inhibition of the 4Fe-4S isoprenoid biosynthesis protein GcpE (IspG)Use of a robot for high-throughput crystallization of membrane proteins in lipidic mesophases.Isoprenoid Biosynthesis in Pathogenic Bacteria: Nuclear Resonance Vibrational Spectroscopy Provides Insight into the Unusual [4Fe-4S] Cluster of the E. coli LytB/IspH Protein.Bioorganometallic chemistry with IspG and IspH: structure, function, and inhibition of the [Fe(4)S(4)] proteins involved in isoprenoid biosynthesis.Current development in isoprenoid precursor biosynthesis and regulation Use of Broken-Symmetry Density Functional Theory To Characterize the IspH Oxidized State: Implications for IspH Mechanism and Inhibition.Pyridine inhibitor binding to the 4Fe-4S protein A. aeolicus IspH (LytB): a HYSCORE Investigation N-Terminal Region of GbIspH1, Ginkgo biloba IspH Type 1, May Be Involved in the pH-Dependent Regulation of Enzyme Activity Study of IspH, a key enzyme in the methylerythritol phosphate pathway using fluoro-substituted substrate analogues Atomic-Resolution Structures of Discrete Stages on the Reaction Coordinate of the [Fe4S4] Enzyme IspG (GcpE)LytB1 and LytB2 of Mycobacterium tuberculosis Are Not Genetically Redundant Structure, function and inhibition of the two- and three-domain 4Fe-4S IspG proteins.Broken-Symmetry DFT Computations for the Reaction Pathway of IspH, an Iron-Sulfur Enzyme in Pathogenic Bacteria A closer look at the spectroscopic properties of possible reaction intermediates in wild-type and mutant (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase.Mechanistic studies of an IspH-catalyzed reaction: implications for substrate binding and protonation in the biosynthesis of isoprenoids.IspH-RPS1 and IspH-UbiA: "Rosetta Stone" Proteins.Biosynthesis of isoprene units: Mössbauer spectroscopy of substrate and inhibitor binding to the [4Fe-4S] cluster of the LytB/IspH enzyme.Inhibition of IspH, a [4Fe-4S]2+ enzyme involved in the biosynthesis of isoprenoids via the methylerythritol phosphate pathway.Terpene biosynthesis: modularity rules Methylerythritol phosphate pathway of isoprenoid biosynthesis.Mechanistic aspects of carotenoid biosynthesis.Molecular cloning and functional identification of a cDNA encoding 4-hydroxy-3-methylbut-2-enyl diphosphate reductase from Tripterygium wilfordii.Convergent strategies in biosynthesis.Biochemistry of the non-mevalonate isoprenoid pathway.Isoprenoids in three-dimensional space: the stereochemistry of terpene biosynthesis.An in silico structural insights into Plasmodium LytB protein and its inhibition.Targeting isoprenoid biosynthesis for drug discovery: bench to bedside Inhibition of the Fe(4)S(4)-cluster-containing protein IspH (LytB): electron paramagnetic resonance, metallacycles, and mechanisms.Mechanistic insights into the reductive dehydroxylation pathway for the biosynthesis of isoprenoids promoted by the IspH enzyme.The amino-terminal conserved domain of 4-hydroxy-3-methylbut-2-enyl diphosphate reductase is critical for its function in oxygen-evolving photosynthetic organisms.

P2860

Q27671864-1326B181-85C7-4D24-89C9-E3C9E77E2166 Q27675866-D6F38454-EF82-47A1-BDD6-9B7DD69485E7 Q27679853-110551B2-A99C-493F-A105-B7305F410EC1 Q27681106-607307EF-C1C7-4385-B99C-2B8321E5C666 Q27683694-A2018D9C-6E07-475E-9AD1-9D055BED1A3F Q27687441-5E84591E-F6CD-4AA9-B0BD-476A2EBD1578 Q28078674-799E046F-707D-4014-8935-0ADCAEF22430 Q28484642-5A0B79CF-66D7-4701-828D-9F7FF242BCC4 Q28537776-AE56591A-8AB0-4768-B612-191D92D6A833 Q28727252-E9F54735-0C7C-4B2A-BA54-F9506BE13BA6 Q28750668-2376937C-EEF4-4984-93A9-A1F911432FFF Q30421196-F7840679-1785-4ACD-BAB0-E36841CD8736 Q30977151-08AF7A03-EB73-432B-A36F-36429288E4B6 Q31149060-BA168F67-0460-40DA-B55B-8B11B7ABCC9E Q33797258-6DE253CD-3F00-4831-A0FF-B18FEA0BEAD5 Q34155674-F33FDE2A-3A93-4953-8316-00BE97FCB5FF Q34972928-376D1120-43CE-4D9A-944F-095AC3622A3C Q35372889-4EBB05AE-EA6C-4529-A42C-A2DBA1C9C7A9 Q35499503-099B64F6-7DEF-4B16-9658-45BF8C141C3C Q35613138-783FA470-3F94-4D00-AB7D-1FC3EC8A6F90 Q35756145-5D23ADD9-335C-4F1D-A19B-41011BA3F008 Q36001278-4D679265-B67F-4BEC-9568-F4F63ADA578F Q36057282-CF9CAE63-8A00-4F16-9742-20768286C612 Q36185966-87A701C2-BDCD-4E74-946C-1911EAAE232A Q36452793-C07DF22F-8033-49A5-B1C4-81FFA89C544D Q36558176-FBAEFDB1-525D-48B8-80FA-45D15D7D48B9 Q36634081-AD0D1868-6609-45E0-9706-25E09F5EA363 Q36817067-F0B448CA-B413-4C39-AD6A-5FAC4C73C28F Q37162126-31C2F876-7FD8-4A1E-AFE8-EF91621EAE2F Q37272872-8E127005-396B-4A59-8285-184139414A67 Q37503777-43FDE148-531F-4B89-8A82-A7D393F25C2E Q37689736-39C4D730-B7B6-47DB-A93A-702A9743A456 Q37872624-DE5917B5-3423-48A9-8CF0-D5261FE77ABB Q37899789-26C541EF-DBAB-496B-B486-430284522622 Q37943241-C950E6C2-9524-43D9-84B2-46947BB1AB4E Q38396474-C1E71203-4650-4BA5-9BB9-13CD68F5AD3C Q39321531-BB540DDA-BA3B-483F-8558-5872CE23FC5F Q40685503-F264CE16-A77F-4124-B30C-87ADDD7178CA Q41025185-50E22087-D53D-47CB-BFB0-C7B45D1F5508 Q41340429-56068111-C1A6-4E84-B645-5545EEB8CC32

P2860

Probing the reaction mechanism of IspH protein by x-ray structure analysis

http://www.wikidata.org/entity/Q27658984

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Probing the reaction mechanism of IspH protein by x-ray structure analysis

@ast

Probing the reaction mechanism of IspH protein by x-ray structure analysis

@en

Probing the reaction mechanism of IspH protein by x-ray structure analysis

@nl

type

label

Probing the reaction mechanism of IspH protein by x-ray structure analysis

@ast

Probing the reaction mechanism of IspH protein by x-ray structure analysis

@en

Probing the reaction mechanism of IspH protein by x-ray structure analysis

@nl

prefLabel

Probing the reaction mechanism of IspH protein by x-ray structure analysis

@ast

Probing the reaction mechanism of IspH protein by x-ray structure analysis

@en

Probing the reaction mechanism of IspH protein by x-ray structure analysis

@nl

P1433

Q27658984-3F342E6B-6FAC-433B-A977-636F779E38FC

P1476

Q27658984-51CC4333-7B07-4A6C-9418-78A7EEC4AB49

P2093

Q27658984-44118200-EBA8-41EC-A7D8-D014EA9E7891

Q27658984-9D1693ED-D699-4A3C-9B8A-490AD29688A3

Q27658984-AA214380-98AD-48FD-A9FF-B4502FBF0747

P2860

Q27658984-0A357DCD-A1E2-4B67-8F43-04E781F4A3A0

Q27658984-1E6FE738-3927-48AE-A208-51D37FAB59E5

Q27658984-44AF2FF6-7109-48AD-A8AA-8E8472F3F094

Q27658984-5482CF84-1DC1-449B-AF91-B9470D845153

Q27658984-6AED03F8-9DAF-4ED4-82D1-56767304043C

Q27658984-80BFCF3B-ED62-4B3A-82D7-93747A335378

Q27658984-92D7DD83-0714-4C48-87BD-76E7B35D2F26

Q27658984-93A318A7-DAEB-4365-BC38-A741160B38C3

Q27658984-94F04CF8-B627-4D75-81B1-A2249369FF99

Q27658984-97543FE3-1B0E-4807-A81D-931F39B32294

P304

Q27658984-EF1AA7DD-C3BA-4BE1-BFAE-326D6ACD88AC

P31

Q27658984-E88785B8-C671-4DDB-ADBD-2F74B9049D64

P3181

Q27658984-38650056-943D-45A4-818B-6EDB3249DC34

P356

Q27658984-0643BABB-0FB6-4C37-8D87-E20DB8C57D97

P407

Q27658984-1547D33F-C825-48E6-9379-983DC79914BF

P433

Q27658984-6AB2BD6D-C96C-4DB6-90D3-644AEE47F228

P478

Q27658984-E0EB111B-FFEE-4EF4-AF5C-4FC258BF18FE

P50

Q27658984-2B514755-8BD2-467E-8FF5-AE9669B56A2A

Q27658984-3786C2CD-3B8D-4BE8-9B3A-9E632D2E34BE

Q27658984-42A72700-95BC-4F3E-BB23-0C6D301A58D2

Q27658984-C299EC43-53BD-481D-9A86-F4EDC2935461

P577

Q27658984-16DEA0E3-2D8E-483C-BDB4-A7712795F907

P5875

Q27658984-914FA11D-3107-43B0-8F53-7E06993EB907

P698

Q27658984-9C39C034-9130-4B4A-B674-D00DDD3BCEB6

P921

Q27658984-EA39C451-C8EF-4D4F-B5DA-0425DAA1B9E9

P932

Q27658984-DC6483AF-2F7D-4CA9-BAEF-3B56F327505C

P3181

P356

PNAS.0913045107

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Probing the reaction mechanism of IspH protein by x-ray structure analysis

@en

P2093

Ingrid Span

http://www.w3.org/2001/XMLSchema#string

Jörg Eppinger

http://www.w3.org/2001/XMLSchema#string

Tobias Gräwert

http://www.w3.org/2001/XMLSchema#string

P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Structure of ( E )-4-Hydroxy-3-methyl-but-2-enyl Diphosphate Reductase, the Terminal Enzyme of the Non-Mevalonate Pathway

Structure of active IspH enzyme from Escherichia coli provides mechanistic insights into substrate reduction

The discovery of a mevalonate-independent pathway for isoprenoid biosynthesis in bacteria, algae and higher plants

Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

Reconstitution of an apicoplast-localised electron transfer pathway involved in the isoprenoid biosynthesis of Plasmodium falciparum

Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein.

IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis.

The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: studies on the mechanisms of the reactions catalyzed by IspG and IspH protein.

Iron-catalyzed reactions in organic synthesis.

P304

1077-81

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

1718619

http://www.w3.org/2001/XMLSchema#string

P356

10.1073/PNAS.0913045107

http://www.w3.org/2001/XMLSchema#string

P407

P433

3

http://www.w3.org/2001/XMLSchema#string

P478

107

http://www.w3.org/2001/XMLSchema#string

P50

Adelbert Bacher

Wolfgang Eisenreich

P577

2010-01-19T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

41040217

http://www.w3.org/2001/XMLSchema#string

P698

20080550

http://www.w3.org/2001/XMLSchema#string

P921

protein structure

P932

2824267

http://www.w3.org/2001/XMLSchema#string